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学術雑誌論文 / Journal Article(1) |
公開日 |
2021-12-21 |
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タイトル |
MPIase is a glycolipozyme essential for membrane protein integration |
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言語 |
eng |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
著者 |
NISHIYAMA, Ken-ichi
MAEDA, Masahide
YANAGISAWA, Kayo
NAGASE, Ryohei
KOMURA, Hajime
IWASHITA, Takashi
YAMAGAKI, Tohru
KUSUMOTO, Shoichi
TOKUDA, Hajime
SHIMAMOTO, Keiko
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著者(機関) |
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値 |
Cryobiofrontier Research Center, Faculty of Agriculture, Iwate University |
著者(機関) |
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Bioorganic Research Institute, Suntory Foundation for Life Sciences |
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Cryobiofrontier Research Center, Faculty of Agriculture, Iwate University |
著者(機関) |
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Bioorganic Research Institute, Suntory Foundation for Life Sciences |
著者(機関) |
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Bioorganic Research Institute, Suntory Foundation for Life Sciences |
著者(機関) |
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Bioorganic Research Institute, Suntory Foundation for Life Sciences |
著者(機関) |
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Bioorganic Research Institute, Suntory Foundation for Life Sciences |
著者(機関) |
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Bioorganic Research Institute, Suntory Foundation for Life Sciences |
著者(機関) |
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Faculty of Nutritional Sciences, The University of Morioka |
著者(機関) |
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値 |
Bioorganic Research Institute, Suntory Foundation for Life Sciences |
登録日 |
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日付 |
2021-12-21 |
書誌情報 |
Nature communications
巻 3,
p. 1260,
発行日 2012-12-11
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ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
20411723 |
抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
Protein integration into biological membranes is a vital cellular event for all organisms. We previously reported an integration factor in the inner membrane of Escherichia coli, named MPIase (membrane protein integrase). Here we show that in contrast to previously identified integration factors that are proteins, MPIase is a glycolipid composed of diacylglycerol and a glycan chain of three acetylated aminosugars linked through pyrophosphate. Hydrolytic removal of the lipid moiety gives a soluble product with higher integration activity than that of the original MPIase. This soluble form of MPIase directly interacts with a newborn membrane protein, maintaining its integration-competent structure and allowing its post-translational integration. MPIase actively drives protein integration following chaperoning membrane proteins. We further demonstrate with anti-MPIase antibodies that MPIase is likely involved in integration in vivo. Collectively, our results suggest that MPIase, essential for membrane protein integration, is to our knowledge the first glycolipid with an enzyme-like activity. |
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出版者 |
Nature Publishing Group |
関係URI |
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識別子タイプ |
URI |
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関連識別子 |
https://www.nature.com/articles/ncomms2267 |
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関連名称 |
MPIase is a glycolipozyme essential for membrane protein integration |
権利 |
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権利情報 |
© 2012 Macmillan Publishers Limited. All rights reserved |
権利URI |
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権利情報 |
http://creativecommons.org/licenses/by-nc-sa/3.0/ |
NCID |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA12645905 |
DOI |
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関連タイプ |
isIdenticalTo |
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識別子タイプ |
DOI |
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関連識別子 |
info:doi/10.1038/ncomms2267 |
著者版フラグ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |